1H–13C hetero-nuclear dipole–dipole couplings of methyl groups in stationary and magic angle spinning solid-state NMR experiments of peptides and proteins
- 28 February 2010
- journal article
- Published by Elsevier in Journal of Magnetic Resonance
- Vol. 202 (2) , 127-134
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopyNature Protocols, 2006
- Recoupling of chemical shift anisotropies in solid-state NMR under high-speed magic-angle spinning and in uniformly C13-labeled systemsThe Journal of Chemical Physics, 2003
- A structural census of genomes: comparing bacterial, eukaryotic, and archaeal genomes in terms of protein structureJournal of Molecular Biology, 1997
- Carbon‐13 chemical shift anisotropies of solid amino acidsMagnetic Resonance in Chemistry, 1993
- Dynamics of fd coat protein in the bacteriophageBiochemistry, 1987
- Dynamics of fd coat protein in lipid bilayersBiochemistry, 1987
- Nuclear magnetic resonance studies of amino acids and proteins. Deuterium nuclear magnetic resonance relaxation of deuteriomethyl-labeled amino acids in crystals and in Halobacterium halobium and Escherichia coli cell membranesBiochemistry, 1984
- Methyl reorientation in polycrystalline amino acids and peptides: a deuteron NMR spin-lattice relaxation studyJournal of the American Chemical Society, 1983
- Solid-state proton relaxation of biomolecular componentsJournal of Magnetic Resonance (1969), 1978
- Proton-enhanced NMR of dilute spins in solidsThe Journal of Chemical Physics, 1973